2XH0

Engineering the enolase active site pocket: Crystal structure of the S39N Q167K D321R mutant of yeast enolase 1

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000015	cellular_component	phosphopyruvate hydratase complex
A	0000287	molecular_function	magnesium ion binding
A	0000324	cellular_component	fungal-type vacuole
A	0004634	molecular_function	phosphopyruvate hydratase activity
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0006096	biological_process	glycolytic process
A	0016829	molecular_function	lyase activity
A	0032889	biological_process	regulation of vacuole fusion, non-autophagic
A	0046872	molecular_function	metal ion binding
A	1904408	molecular_function	melatonin binding
B	0000015	cellular_component	phosphopyruvate hydratase complex
B	0000287	molecular_function	magnesium ion binding
B	0000324	cellular_component	fungal-type vacuole
B	0004634	molecular_function	phosphopyruvate hydratase activity
B	0005737	cellular_component	cytoplasm
B	0005739	cellular_component	mitochondrion
B	0005829	cellular_component	cytosol
B	0005886	cellular_component	plasma membrane
B	0006096	biological_process	glycolytic process
B	0016829	molecular_function	lyase activity
B	0032889	biological_process	regulation of vacuole fusion, non-autophagic
B	0046872	molecular_function	metal ion binding
B	1904408	molecular_function	melatonin binding
C	0000015	cellular_component	phosphopyruvate hydratase complex
C	0000287	molecular_function	magnesium ion binding
C	0000324	cellular_component	fungal-type vacuole
C	0004634	molecular_function	phosphopyruvate hydratase activity
C	0005737	cellular_component	cytoplasm
C	0005739	cellular_component	mitochondrion
C	0005829	cellular_component	cytosol
C	0005886	cellular_component	plasma membrane
C	0006096	biological_process	glycolytic process
C	0016829	molecular_function	lyase activity
C	0032889	biological_process	regulation of vacuole fusion, non-autophagic
C	0046872	molecular_function	metal ion binding
C	1904408	molecular_function	melatonin binding
D	0000015	cellular_component	phosphopyruvate hydratase complex
D	0000287	molecular_function	magnesium ion binding
D	0000324	cellular_component	fungal-type vacuole
D	0004634	molecular_function	phosphopyruvate hydratase activity
D	0005737	cellular_component	cytoplasm
D	0005739	cellular_component	mitochondrion
D	0005829	cellular_component	cytosol
D	0005886	cellular_component	plasma membrane
D	0006096	biological_process	glycolytic process
D	0016829	molecular_function	lyase activity
D	0032889	biological_process	regulation of vacuole fusion, non-autophagic
D	0046872	molecular_function	metal ion binding
D	1904408	molecular_function	melatonin binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 1439

Chain	Residue
A	ASP246
A	GLU295
A	ASP320
A	PEP1440
A	HOH2302

---

site_id	AC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE PEP A 1440

Chain	Residue
A	ASP246
A	GLU295
A	ASP320
A	ARG321
A	LEU343
A	LYS345
A	HIS373
A	ARG374
A	SER375
A	LYS396
A	MG1439
A	GLY37
A	ALA38
A	LYS167
A	GLU168

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 1439

Chain	Residue
B	ASP246
B	GLU295
B	ASP320
B	PEP1440
B	HOH2277

---

site_id	AC4
Number of Residues	15
Details	BINDING SITE FOR RESIDUE PEP B 1440

Chain	Residue
B	GLY37
B	ALA38
B	LYS167
B	GLU168
B	ASP246
B	GLU295
B	ASP320
B	ARG321
B	LEU343
B	LYS345
B	ARG374
B	SER375
B	LYS396
B	MG1439
B	HOH2411

---

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG C 1439

Chain	Residue
C	ASP246
C	GLU295
C	ASP320
C	ARG321
C	PEP1440
C	HOH2271

---

site_id	AC6
Number of Residues	17
Details	BINDING SITE FOR RESIDUE PEP C 1440

Chain	Residue
C	GLY37
C	ALA38
C	LYS167
C	GLU168
C	GLU211
C	ASP246
C	GLU295
C	ASP320
C	ARG321
C	LEU343
C	LYS345
C	HIS373
C	ARG374
C	SER375
C	LYS396
C	MG1439
C	HOH2405

---

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG D 1439

Chain	Residue
D	ASP246
D	GLU295
D	ASP320
D	PEP1440
D	HOH2192

---

site_id	AC8
Number of Residues	16
Details	BINDING SITE FOR RESIDUE PEP D 1440

Chain	Residue
D	GLY37
D	ALA38
D	LYS167
D	GLU168
D	ASP246
D	GLU295
D	ASP320
D	ARG321
D	LEU343
D	LYS345
D	HIS373
D	ARG374
D	SER375
D	LYS396
D	MG1439
D	HOH2304

---

Functional Information from PROSITE/UniProt

site_id	PS00164
Number of Residues	14
Details	ENOLASE Enolase signature. LLLKvNQIGTLSES

Chain	Residue	Details
A	LEU342-SER355

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton donor => ECO:0000269|PubMed:12846578

Chain	Residue	Details
A	GLU211
B	GLU211
C	GLU211
D	GLU211

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000269|PubMed:12846578, ECO:0000269|PubMed:8634301

Chain	Residue	Details
A	LYS345
B	LYS345
C	LYS345
D	LYS345

---

site_id	SWS_FT_FI3
Number of Residues	20
Details	BINDING: BINDING => ECO:0000269|PubMed:8605183, ECO:0000269|PubMed:9376357

Chain	Residue	Details
A	HIS159
B	LYS396
C	HIS159
C	GLU168
C	GLU295
C	ASP320
C	LYS396
D	HIS159
D	GLU168
D	GLU295
D	ASP320
A	GLU168
D	LYS396
A	GLU295
A	ASP320
A	LYS396
B	HIS159
B	GLU168
B	GLU295
B	ASP320

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:8605183

Chain	Residue	Details
A	ASP246
B	ASP246
C	ASP246
D	ASP246

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:12054465, ECO:0000269|PubMed:8605183, ECO:0000269|PubMed:9376357

Chain	Residue	Details
A	SER372
B	SER372
C	SER372
D	SER372

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:17287358

Chain	Residue	Details
A	SER118
B	SER118
C	SER118
D	SER118

---

site_id	SWS_FT_FI7
Number of Residues	8
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P00925

Chain	Residue	Details
A	SER137
A	SER187
B	SER137
B	SER187
C	SER137
C	SER187
D	SER137
D	SER187

---

site_id	SWS_FT_FI8
Number of Residues	8
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P00925

Chain	Residue	Details
A	THR312
A	THR323
B	THR312
B	THR323
C	THR312
C	THR323
D	THR312
D	THR323

---

site_id	SWS_FT_FI9
Number of Residues	8
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P00925

Chain	Residue	Details
A	LYS59
A	LYS242
B	LYS59
B	LYS242
C	LYS59
C	LYS242
D	LYS59
D	LYS242

---

site_id	SWS_FT_FI10
Number of Residues	8
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047

Chain	Residue	Details
A	LYS357
B	LYS357
C	LYS357
D	LYS357

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	10
Details	M-CSA 311

Chain	Residue	Details
A	ASN39	metal ligand
A	LYS396	electrostatic stabiliser, hydrogen bond donor, proton shuttle (general acid/base)
A	HIS159	electrostatic stabiliser, proton shuttle (general acid/base)
A	GLU168	activator, electrostatic stabiliser, hydrogen bond acceptor, increase acidity, repulsive charge-charge interaction
A	GLU211	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton donor
A	ASP246	metal ligand
A	GLU295	metal ligand
A	ASP320	metal ligand
A	LYS345	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor
A	HIS373	electrostatic stabiliser, hydrogen bond donor

---

site_id	MCSA2
Number of Residues	10
Details	M-CSA 311

Chain	Residue	Details
B	ASN39	metal ligand
B	LYS396	electrostatic stabiliser, hydrogen bond donor, proton shuttle (general acid/base)
B	HIS159	electrostatic stabiliser, proton shuttle (general acid/base)
B	GLU168	activator, electrostatic stabiliser, hydrogen bond acceptor, increase acidity, repulsive charge-charge interaction
B	GLU211	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton donor
B	ASP246	metal ligand
B	GLU295	metal ligand
B	ASP320	metal ligand
B	LYS345	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor
B	HIS373	electrostatic stabiliser, hydrogen bond donor

---

site_id	MCSA3
Number of Residues	10
Details	M-CSA 311

Chain	Residue	Details
C	ASN39	metal ligand
C	LYS396	electrostatic stabiliser, hydrogen bond donor, proton shuttle (general acid/base)
C	HIS159	electrostatic stabiliser, proton shuttle (general acid/base)
C	GLU168	activator, electrostatic stabiliser, hydrogen bond acceptor, increase acidity, repulsive charge-charge interaction
C	GLU211	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton donor
C	ASP246	metal ligand
C	GLU295	metal ligand
C	ASP320	metal ligand
C	LYS345	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor
C	HIS373	electrostatic stabiliser, hydrogen bond donor

---

site_id	MCSA4
Number of Residues	10
Details	M-CSA 311

Chain	Residue	Details
D	ASN39	metal ligand
D	LYS396	electrostatic stabiliser, hydrogen bond donor, proton shuttle (general acid/base)
D	HIS159	electrostatic stabiliser, proton shuttle (general acid/base)
D	GLU168	activator, electrostatic stabiliser, hydrogen bond acceptor, increase acidity, repulsive charge-charge interaction
D	GLU211	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton donor
D	ASP246	metal ligand
D	GLU295	metal ligand
D	ASP320	metal ligand
D	LYS345	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor
D	HIS373	electrostatic stabiliser, hydrogen bond donor

---